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PDBsum entry 1ywi
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Structural protein
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PDB id
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1ywi
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References listed in PDB file
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Key reference
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Title
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Structural basis for apptppplpp peptide recognition by the fbp11ww1 domain.
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Authors
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J.R.Pires,
C.Parthier,
R.Aido-Machado,
U.Wiedemann,
L.Otte,
G.Böhm,
R.Rudolph,
H.Oschkinat.
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Ref.
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J Mol Biol, 2005,
348,
399-408.
[DOI no: ]
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PubMed id
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Abstract
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WW domains are small protein-protein interaction modules that recognize
proline-rich stretches in proteins. The class II tandem WW domains of the formin
binding protein 11 (FBP11) recognize specifically proteins containing PPLPp
motifs as present in the formins that are involved in limb and kidney
development, and in the methyl-CpG-binding protein 2 (MeCP2), associated with
the Rett syndrome. The interaction involves the specific recognition of a
leucine side-chain. Here, we report on the novel structure of the complex formed
by the FPB11WW1 domain and the formin fragment APPTPPPLPP revealing the
specificity determinants of class II WW domains.
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Figure 1.
Figure 1. The WW domain sequences and classes. Amino acid
sequence of selected WW domains grouped in classes according to
ligand specificity.4 Classes/ligand motifs: class II PPLPp
(magenta), class III (p/  )P(p/g)PPpR
or (p/ )PPRgpPp
(orange), class IV (poS/poT)P (green) and class I PPxY (blue).
Conserved amino acid residues are in bold; amino acid residues
on the b-strand face where binding occurs are grey-shaded; amino
acid residues responsible for class specificity are colored. The
asterisk (*) indicates sequences assumed to be FBP11 orthologs.
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Figure 4.
Figure 4. Comparison of WW and SH3 domain complexes. (a)
Schematic representation of a WW domain showing important
regions for ligand recognition. Residues conserved for all WW
domains are displayed in blue. Positions changing between the WW
domain specificity classes are shown in green, next to which the
amino acid types and their corresponding WW domain classes are
indicated in parentheses. Superposition of FBP11WW1 (grey
ribbon, blue side-chains, class II) complexed to APPTPPPLPP
(cyan) with: (b) dystrophinWW domain (red, class I) in complex
with SPPPY (yellow); (c) Pin1WW domain (red, class IV): in
complex with (poS)PT(poS)PS (yellow); and (d) the C-CRK
N-terminal SH3 domain (red) in complex with PPPALPPK (yellow).
(e) PRP40WW1 (red, class II) and (f) PRP40WW2 (red, class II)
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2005,
348,
399-408)
copyright 2005.
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